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- W2002246210 abstract "TFIID is an essential factor required for RNA polymerase II transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a structural analysis of the TAF5 protein. Our structure at 2.2-Å resolution of the TAF5-NTD2 domain reveals an α-helical domain with distant structural similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain contains several conserved clefts likely to be critical for TFIID complex assembly. Our biochemical analysis of the human TAF5 protein demonstrates the ability of the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a key property required for the assembly of the TFIID complex." @default.
- W2002246210 created "2016-06-24" @default.
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- W2002246210 date "2007-01-23" @default.
- W2002246210 modified "2023-09-27" @default.
- W2002246210 title "Structural analysis and dimerization potential of the human TAF5 subunit of TFIID" @default.
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- W2002246210 doi "https://doi.org/10.1073/pnas.0610297104" @default.
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